ID A0A7K5ZYJ8_ONYCO Unreviewed; 951 AA.
AC A0A7K5ZYJ8;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 20.
DE RecName: Full=Ephrin type-B receptor 2 {ECO:0000256|ARBA:ARBA00070277};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=EPH-like kinase 5 {ECO:0000256|ARBA:ARBA00076438};
DE Flags: Fragment;
GN Name=Ephb1 {ECO:0000313|EMBL:NWU82770.1};
GN ORFNames=ONYCOR_R03473 {ECO:0000313|EMBL:NWU82770.1};
OS Onychorhynchus coronatus (Royal flycatcher).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Tyrannidae; Onychorhynchus.
OX NCBI_TaxID=360224 {ECO:0000313|EMBL:NWU82770.1, ECO:0000313|Proteomes:UP000550309};
RN [1] {ECO:0000313|EMBL:NWU82770.1, ECO:0000313|Proteomes:UP000550309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-028-75 {ECO:0000313|EMBL:NWU82770.1};
RC TISSUE=Mixed tissue sample {ECO:0000313|EMBL:NWU82770.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC transmembrane ephrin-B family ligands residing on adjacent cells,
CC leading to contact-dependent bidirectional signaling into neighboring
CC cells. The signaling pathway downstream of the receptor is referred to
CC as forward signaling while the signaling pathway downstream of the
CC ephrin ligand is referred to as reverse signaling. Functions in axon
CC guidance during development. In addition to axon guidance, also
CC regulates dendritic spines development and maturation and stimulates
CC the formation of excitatory synapses. {ECO:0000256|ARBA:ARBA00055849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses.
CC {ECO:0000256|ARBA:ARBA00038546}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection,
CC dendrite {ECO:0000256|ARBA:ARBA00004279}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NWU82770.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VZRK01000195; NWU82770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K5ZYJ8; -.
DR OrthoDB; 4062651at2759; -.
DR Proteomes; UP000550309; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IEA:TreeGrafter.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR CDD; cd09551; SAM_EPH-B1; 1.
DR FunFam; 2.60.40.10:FF:000041; ephrin type-A receptor 3; 1.
DR FunFam; 1.10.150.50:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.10.50.10:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.60.40.1770:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 3.30.200.20:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 1.10.510.10:FF:000015; Ephrin type-B receptor 2; 1.
DR FunFam; 2.60.120.260:FF:000004; Ephrin type-B receptor 2; 1.
DR FunFam; 2.60.40.10:FF:000110; Ephrin type-B receptor 2; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR042819; EphB1_SAM.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR050449; Ephrin_rcpt_TKs.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF17; EPHRIN TYPE-B RECEPTOR 1; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF25599; Ephrin_CRD; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000550309};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 508..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..160
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 281..391
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 392..495
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 586..849
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 878..942
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 711
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 592..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 20..142
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 55..65
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWU82770.1"
FT NON_TER 951
FT /evidence="ECO:0000313|EMBL:NWU82770.1"
SQ SEQUENCE 951 AA; 106410 MW; 4039ECA19B8743CE CRC64;
WEEVSGYDEN LNTIRTYQVC NVFEPNQNNW LLTTFINRRG AHRIYTEMRF TVRDCSSLPN
VPGSCKETFN LYYYETDSVI ATKKSTFWTE APYLKVDTIA ADESFSQVDF GGRLMKVNTE
VRSFGPLTRN GFYLAFQDYG ACMSLLSVRV FFKKCPSVVQ NFAIFPETMT GAESTSLVTA
RGTCIPNAEE VDVPIKLYCN GDGEWMVPIG RCTCKAGYEP ENNVACKACP AGTFKASQGA
GVCVPCPPNS RSTAEASPVC ACRNGYYRAD FDPPAAACTS VPSGPRNVIS IVNETSIILE
WHPPRETGGR DDVTYNIVCK KCRSDRRACS RCDDNVDFVP RQLGLTDTRV FISNLWAHTP
YTFEIQAVNG VSNKSPFPQQ HVSVNITTNQ AAPSTVPIMH QVSATMRSIT LSWPQPEQPN
GIILDYEIRY YEKLSRICTP DDHNEYNSSM ARSQTNTARI EGLRPGMVYV VQVRARTVAG
YGKYSGKMCF QTLTDDDYKS ELREQLPLIA GSAAAGVVFI VSLVAISIVC SRKRAYSKEA
VYSDKLQHYS TGRGSPGMKI YIDPFTYEDP NEAVREFAKE IDVSFVKIEE VIGAGEFGEV
YKGRLKLPGK REIYVAIKTL KAGYSEKQRR DFLSEASIMG QFDHPNIIRL EGVVTKSRPV
MIITEFMENG ALDSFLRQND GQFTVIQLVG MLRGIAAGMK YLAEMNYVHR DLAARNILVN
SNLVCKVSDF GLSRYLQDDT SDPTYTSSLG GKIPVRWTAP EAIAYRKFTS ASDVWSYGIV
MWEVMSFGER PYWDMSNQDV INAIEQDYRL PPPMDCPAAL HQLMLDCWQK DRNTRPRFTE
IVNTLDKMIR NPASLKTVAT ITAVPSQPLL DRSIPDFTAF TSVDDWLSAV KMSQYRDSFL
TAGFTSLQLV AQMTSEDLLR IGVTLAGHQK KILNSVQSMR VQMSQSPTSM A
//
